MolNFT v1 · #116680 · protein

Crystal structure of glucosidase II alpha subunit (GLC1MAN2-bound from)

5DL0 · Alpha glucosidase-like protein: “Crystal structure of glucosidase II alpha subunit (GLC1MAN2-bound from)”. X-ray diffraction, 2 ligands (MAN, GLC), 12 pockets (best druggability 0.68). MolNFT v1 #116680 on GenesisL1: 3D structure…

PDB: 5DL0
Type: protein
Length: 924 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha glucosidase-like protein
UniProt: G0SG42
Ligands: MAN, GLC
Pockets: 12 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha glucosidase-like protein	protein	924	22% helix, 29% strand	G0SG42

Ligands and binding sites

MAN · alpha-D-mannopyranose · sugar · chains A
GLC · alpha-D-glucopyranose · sugar · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.68	0.96	29	empty
2	138	0.62	0.85	22	MAN, GLC
3	212	0.53	0.78	35	empty
4	70	0.51	0.86	17	empty
5	106	0.42	0.77	28	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5DL0 · Crystal structure of glucosidase II alpha subunit (Glc1Man2-bound from) · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt G0SG42
Elsewhere: RCSB PDB 5DL0 · PDBe 5DL0 · UniProt G0SG42

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